Heat Shock Proteins and Ferroptosis

Abstract

Ferroptosis is a new form of regulatory cell death named by Dixon in 2012, which is characterized by the accumulation of lipid peroxides and iron ions. Molecular chaperones are a class of evolutionarily conserved proteins in the cytoplasm. They recognize and bind incompletely folded or assembled proteins to help them fold, transport or prevent their aggregation, but they themselves do not participate in the formation of final products. As the largest number of molecular chaperones, heat shock proteins can be divided into five families: HSP110 (HSPH), HSP90 (HSPC), HSP70 (HSPA), HSP40 (DNAJ) and small heat shock proteins (HSPB). Different heat shock proteins play different roles in promoting or inhibiting ferroptosis in different diseases. It is known that ferroptosis is participated in tumors, nervous system diseases, renal injury and ischemia-reperfusion injury. However, there are few reviews about the relationship of heat shock proteins and ferroptosis. In this study, we systematically summarize the roles of heat shock proteins in the occurrence of ferroptosis, and predict the possible mechanisms of different families of heat shock proteins in the development of ferroptosis.

Increased ATF2 expression predicts poor prognosis and inhibits sorafenib-induced ferroptosis in gastric cancer

“…Given the prominent role of heat shock proteins in ferroptosis reported by several studies [ 22 ], we sought to determine whether HSPH1 might affect SLC7A11 expression in GC. We first queried the GeneMANIA database, and the potential interactions between HSPH1 and SLC7A11 were predicted and displayed ( Fig.…”

Heat stress inhibits the proliferation and differentiation of myoblasts and is associated with damage to mitochondria

“…ROS is a highly active molecule derived from oxygen that maintains the stability of the organism and partakes in the signal transduction of cell metabolism ( Postiglione and Muday, 2020 ; Liu et al, 2022 ). Exogenous stimulation facilitates the production of cellular ROS ( Kasai et al, 2020 ).…”

Preparation and Application Analysis of a Polyclonal Antibody as Reference Protein in Helicoverpa armigera (Lepidoptera: Noctuidae)

“…Their function under normal physiological conditions is to help proteins fold, assemble, operate, and degrade properly. Under stress conditions, they stabilize protein and membrane structures, prevent denatured protein aggregation, and help proteins refold (Androvitsanea et al 2021; Liu et al 2022b; Roque 2022). To date, only a few studies have examined the heat shock protein family as reference proteins.…”